Reviewed, UniProtKB/Swiss-Prot Q8VI36 (PAXI_MOUSE)

Names and origin

Protein names

Recommended name:
    Paxillin

Gene names

Name:

Pxn

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion) By similarity.
Subunit structure	Binds to vinculin, to the SH3 domain of c-SRC and to focal adhesion kinase. Interacts with GIT1, NUDT16L1/SDOS and TGFB1I1. Component of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and PAK1. Binds ASAP2. Interacts with RNF5 By similarity. Interacts with PARVA.
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cell junction › focal adhesion By similarity.
Post-translational modification	Phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens By similarity.
Sequence similarities	Belongs to the paxillin family. Contains 4 LIM zinc-binding domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	activation of MAPK activity Inferred from direct assay. Source: MGI branching morphogenesis of a tube Inferred from direct assay. Source: MGI cell motion Inferred from mutant phenotype. Source: MGI cytoskeleton organization Inferred from mutant phenotype. Source: MGI focal adhesion formation Inferred from direct assay. Source: MGI integrin-mediated signaling pathway Ref.1 Inferred from mutant phenotype. Source: MGI lamellipodium assembly Inferred from direct assay. Source: MGI peptidyl-tyrosine phosphorylation Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Ref.1 Inferred from direct assay. Source: MGI lamellipodium Inferred from direct assay. Source: MGI
Molecular function	BH4 domain binding Inferred from physical interaction. Source: MGI receptor signaling complex scaffold activity Traceable author statement. Source: MGI zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ptk2	P34152	1	EBI-983394,EBI-77070

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Beta (identifier: Q8VI36-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Alpha (identifier: Q8VI36-2)

The sequence of this isoform differs from the canonical sequence as follows:
     278-311: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 591	591	Paxillin		PRO_0000075854
Regions
	Domain	356 – 415	60	LIM zinc-binding 1
	Domain	416 – 473	58	LIM zinc-binding 2
	Domain	474 – 533	60	LIM zinc-binding 3
	Domain	534 – 591	58	LIM zinc-binding 4
	Motif	3 – 15	13	LD motif 1
	Motif	144 – 156	13	LD motif 2
	Motif	216 – 228	13	LD motif 3
	Motif	265 – 276	12	LD motif 4
	Motif	333 – 345	13	LD motif 5
	Compositional bias	46 – 53	8	Pro-rich
Amino acid modifications
	Modified residue	31	1	Phosphotyrosine By similarity
	Modified residue	83	1	Phosphoserine
	Modified residue	88	1	Phosphotyrosine
	Modified residue	106	1	Phosphoserine By similarity
	Modified residue	109	1	Phosphoserine By similarity
	Modified residue	118	1	Phosphotyrosine Ref.4
	Modified residue	126	1	Phosphoserine By similarity
	Modified residue	130	1	Phosphoserine By similarity
	Modified residue	137	1	Phosphoserine By similarity
	Modified residue	181	1	Phosphotyrosine By similarity
	Modified residue	303	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	278 – 311	34	Missing in isoform Alpha.		VSP_016357
Experimental info
	Sequence conflict	71	1	P → R in BAE42452. Ref.2
	Sequence conflict	212	1	D → N in BAE34151. Ref.2
	Sequence conflict	294	1	G → S in BAE34151. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta [UniParc]. Last modified March 1, 2002. Version 1. Checksum: B41A1892E6F60544	FASTA	591	64,476
	10 20 30 40 50 60 MDDLDALLAD LESTTSHISK RPVFLSEEPP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG 70 80 90 100 110 120 TVLDPLDQWQ PSGSRYAHQQ PPSPLPVYSS SAKNSSASNT QDGVGSLCSR AGEEEHVYSF 130 140 150 160 170 180 PNKQKSAEPS PTVMSSSLGS NLSELDRLLL ELNAVQHSPP GFPADEAESS PPLPGALSPL 190 200 210 220 230 240 YGIPENNTPL GGKAGPLVKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG 250 260 270 280 290 300 EMSSPQRVTS SQQQTRISAS SATRELDELM ASLSDFKMQG LEQRVDGERP WAAGWPPSSR 310 320 330 340 350 360 QSSPEGQDEG GFMAQGKTGS SSPPGGLSKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA 370 380 390 400 410 420 CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD GQPYCEKDYH SLFSPRCYYC 430 440 450 460 470 480 NGPILDKVVT ALDRTWHPEH FFCAQCGAFF GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA 490 500 510 520 530 540 RAILENYISA LNTLWHPECF VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK 550 560 570 580 590 PITGRCITAM AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQSCFVKLF C
	Isoform Alpha. Checksum: 483D880CF16289B5	FASTA	557	60,811
	10 20 30 40 50 60 MDDLDALLAD LESTTSHISK RPVFLSEEPP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG 70 80 90 100 110 120 TVLDPLDQWQ PSGSRYAHQQ PPSPLPVYSS SAKNSSASNT QDGVGSLCSR AGEEEHVYSF 130 140 150 160 170 180 PNKQKSAEPS PTVMSSSLGS NLSELDRLLL ELNAVQHSPP GFPADEAESS PPLPGALSPL 190 200 210 220 230 240 YGIPENNTPL GGKAGPLVKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG 250 260 270 280 290 300 EMSSPQRVTS SQQQTRISAS SATRELDELM ASLSDFKFMA QGKTGSSSPP GGLSKPGSQL 310 320 330 340 350 360 DSMLGSLQSD LNKLGVATVA KGVCGACKKP IAGQVVTAMG KTWHPEHFVC THCQEEIGSR 370 380 390 400 410 420 NFFERDGQPY CEKDYHSLFS PRCYYCNGPI LDKVVTALDR TWHPEHFFCA QCGAFFGPEG 430 440 450 460 470 480 FHEKDGKAYC RKDYFDMFAP KCGGCARAIL ENYISALNTL WHPECFVCRE CFTPFVNGSF 490 500 510 520 530 540 FEHDGQPYCE VHYHERRGSL CSGCQKPITG RCITAMAKKF HPEHFVCAFC LKQLNKGTFK 550 EQNDKPYCQS CFVKLFC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Linkage of caspase-mediated degradation of paxillin to apoptosis in Ba/F3 murine pro-B lymphocytes." Chay K.O., Park S.S., Mushinski J.F. J. Biol. Chem. 277:14521-14529(2002) [PubMed: 11825902] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA). Strain: BALB/c. Tissue: Testis.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA). Strain: C57BL/6J and NOD. Tissue: Placenta and Spleen.
[3]	"Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion." Nikolopoulos S.N., Turner C.E. J. Cell Biol. 151:1435-1448(2000) [PubMed: 11134073] [Abstract] Cited for: INTERACTION WITH PARVA.
[4]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; TYR-88 AND TYR-118, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF293883 mRNA. Translation: AAL71910.1. AF293882 mRNA. Translation: AAL71909.1. AK149933 mRNA. Translation: BAE29176.1. AK157688 mRNA. Translation: BAE34151.1. AK167299 mRNA. Translation: BAE39404.1. AK171436 mRNA. Translation: BAE42452.1.
IPI	IPI00128703. IPI00165881.
UniGene	Mm.18714
3D structure databases
HSSP	HSSP built from PDB template 1NYP based on UniProtKB P48059.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8VI36. 3 interactions.
PTM databases
PhosphoSite	Q8VI36.
Proteomic databases
PRIDE	Q8VI36.
Genome annotation databases
Ensembl	ENSMUSG00000029528. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:108295. Pxn.
Phylogenomic databases
HOGENOM	Q8VI36.
HOVERGEN	Q8VI36.
Gene expression databases
ArrayExpress	Q8VI36.
Bgee	Q8VI36.
CleanEx	MM_PXN.
GermOnline	ENSMUSG00000029528. Mus musculus.
Family and domain databases
InterPro	IPR001904. Paxillin. IPR001781. Znf_LIM. [Graphical view]
Gene3D	G3DSA:2.10.110.10. Znf_LIM. 3 hits.
Pfam	PF00412. LIM. 4 hits. PF03535. Paxillin. 1 hit. [Graphical view]
PRINTS	PR00832. PAXILLIN.
ProDom	PD000094. LIM. 4 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00132. LIM. 4 hits. [Graphical view]
PROSITE	PS00478. LIM_DOMAIN_1. 4 hits. PS50023. LIM_DOMAIN_2. 4 hits. [Graphical view]
ProtoNet	Search...
Other Resources
PMAP-CutDB	Q8VI36.
SOURCE	Search...

Entry information

Entry name

PAXI_MOUSE

Accession

Primary (citable) accession number: Q8VI36
Secondary accession number(s): Q3TB62, Q3TZQ6, Q8VI37

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	March 1, 2002
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)